Research workbench
ATPase domain D3 of the essc coupling protein from S. aureus USA300
Analyse ATPase domain D3 of the essc coupling protein from S. aureus USA300 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6TV1
- Type
- protein
- Length
- 228 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Essc protein
- UniProt
- A0A0H2XEV3
- Pockets
- 1 · best druggability 0.29
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Essc protein | protein | 228 | 42% helix, 26% strand | A0A0H2XEV3 |
Ligands and binding sites
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 69 | 0.29 | 0.73 | 16 | empty |
Compared structures
- 6TV1 · ATPase domain D3 of the EssC coupling protein from S. aureus USA300 · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt A0A0H2XEV3
- Elsewhere: RCSB PDB 6TV1 · PDBe 6TV1 · UniProt A0A0H2XEV3
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